ID   ODPA_KLULA              Reviewed;         412 AA.
AC   O13366; Q6CKB5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   Name=PDA1; OrderedLocusNames=KLLA0F12001g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC MYA-539 / JBD100;
RX   PubMed=9884236; DOI=10.1099/00221287-144-12-3437;
RA   Zeeman A.-M., Luttik M.A.H., Thiele C., van Dijken J.P., Pronk J.T.,
RA   Steensma H.Y.;
RT   "Inactivation of the Kluyveromyces lactis KlPDA1 gene leads to loss of
RT   pyruvate dehydrogenase activity, impairs growth on glucose and triggers
RT   aerobic alcoholic fermentation.";
RL   Microbiology 144:3437-3446(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC         acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: E1 activity is regulated by phosphorylation
CC       (inactivation) and dephosphorylation (activation) of the alpha subunit.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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DR   EMBL; AF023920; AAD03773.1; -; Genomic_DNA.
DR   EMBL; CR382126; CAG98332.1; -; Genomic_DNA.
DR   RefSeq; XP_455624.1; XM_455624.1.
DR   AlphaFoldDB; O13366; -.
DR   SMR; O13366; -.
DR   STRING; 284590.O13366; -.
DR   PaxDb; 284590-O13366; -.
DR   GeneID; 2894999; -.
DR   KEGG; kla:KLLA0_F12001g; -.
DR   eggNOG; KOG0225; Eukaryota.
DR   HOGENOM; CLU_029393_5_2_1; -.
DR   InParanoid; O13366; -.
DR   OMA; HGIVGGQ; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03182; PDH_E1_alph_y; 1.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   3: Inferred from homology;
KW   Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate;
KW   Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..412
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha,
FT                   mitochondrial"
FT                   /id="PRO_0000020450"
FT   CONFLICT        275..281
FT                   /note="YQASKFA -> TKL (in Ref. 1; AAD03773)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   412 AA;  45453 MW;  CBCC8AB3DC4C7E96 CRC64;
     MLSLKAQSSV VGKSSSLRLV RNFSKNVRAL SQVADETKPG DDDLVQIDLP ETSFEGYLLD
     VPELSYQTTK SNLLQMYKDM IIVRRMEMAC DALYKAKKIR GFCHSSVGQE AIAVGIENAI
     TKRDTVITSY RCHGFTYMRG AAVQAVLAEL MGRRTGVSFG KGGSMHLYAP GFYGGNGIVG
     AQVPLGAGLA FAHQYKHEDA CSFALYGDGA SNQGQVFESF NMAKLWNLPA VFCCENNKYG
     MGTAAARSSA MTEYFKRGQY IPGLKVNGMD ILAVYQASKF AKDWTVSGNG PIVLEYETYR
     YGGHSMSDPG TTYRTRDEIQ HMRSKNDPIA GLKMHLLELG IATEDEIKAY DKAARKYVDE
     QVELADAAPA PEAKMSILFE DVYVPGSETP TLRGRLQEDT WDFAKKSFAF RD
//